ID ENLYS_BPT3 Reviewed; 151 AA. AC P20331; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 106. DE RecName: Full=Endolysin {ECO:0000255|HAMAP-Rule:MF_04111}; DE EC=3.5.1.28 {ECO:0000255|HAMAP-Rule:MF_04111}; DE AltName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000255|HAMAP-Rule:MF_04111}; DE AltName: Full=T3 lysozyme; GN Name=3.5; OS Enterobacteria phage T3 (Bacteriophage T3). OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Autographiviridae; Studiervirinae; Teetrevirus; Teetrevirus T3Luria. OX NCBI_TaxID=10759; OH NCBI_TaxID=562; Escherichia coli. RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Luria; RX PubMed=2614843; DOI=10.1016/0022-2836(89)90102-2; RA Beck P.J., Gonzalez S., Ward C.L., Molineux I.J.; RT "Sequence of bacteriophage T3 DNA from gene 2.5 through gene 9."; RL J. Mol. Biol. 210:687-701(1989). CC -!- FUNCTION: Plays an important role in the switch between viral CC transcription and genome replication. Once produced in sufficient CC amount, interacts with and inhibits the viral RNA polymerase that CC becomes unable to produce additional late transcripts. This lysozyme- CC polymerase complex in turn plays an active role in viral genome CC replication and packaging. {ECO:0000255|HAMAP-Rule:MF_04111}. CC -!- FUNCTION: Endolysin with amidase activity that degrades host CC peptidoglycans and participates with the holin and spanin proteins in CC the sequential events which lead to the programmed host cell lysis CC releasing the mature viral particles. Once the holin has permeabilized CC the host cell membrane, the endolysin can reach the periplasm and CC breaking down the peptidoglycan layer. {ECO:0000255|HAMAP- CC Rule:MF_04111}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L- CC amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28; CC Evidence={ECO:0000255|HAMAP-Rule:MF_04111}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_04111}; CC Note=Zn(2+) is required for amidase activity. {ECO:0000255|HAMAP- CC Rule:MF_04111}; CC -!- ACTIVITY REGULATION: Binding to the viral RNA polymerase inhibits CC amidase activity. {ECO:0000255|HAMAP-Rule:MF_04111}. CC -!- SUBUNIT: Interacts with the viral RNA polymerase. {ECO:0000255|HAMAP- CC Rule:MF_04111}. CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04111}. CC Note=The endolysin is cytoplasmic, but can reach the periplasmic space CC with the help of the holins which disrupt the host cell membrane. CC {ECO:0000255|HAMAP-Rule:MF_04111}. CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. CC {ECO:0000255|HAMAP-Rule:MF_04111}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X17255; CAA35133.1; -; Genomic_DNA. DR PIR; S07506; S07506. DR RefSeq; NP_523313.1; NC_003298.1. DR SMR; P20331; -. DR GeneID; 927411; -. DR KEGG; vg:927411; -. DR OrthoDB; 13080at10239; -. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW. DR GO; GO:0032897; P:negative regulation of viral transcription; IEA:InterPro. DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0044659; P:viral release from host cell by cytolysis; IEA:UniProtKB-UniRule. DR CDD; cd06583; PGRP; 1. DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1. DR HAMAP; MF_04111; ENDOLYSIN_T7; 1. DR InterPro; IPR036505; Amidase/PGRP_sf. DR InterPro; IPR002502; Amidase_domain. DR InterPro; IPR034689; Endolysin_T7_type. DR InterPro; IPR015510; PGRP. DR InterPro; IPR006619; PGRP_domain_met/bac. DR PANTHER; PTHR11022; PEPTIDOGLYCAN RECOGNITION PROTEIN; 1. DR PANTHER; PTHR11022:SF41; PEPTIDOGLYCAN-RECOGNITION PROTEIN SC1A-RELATED; 1. DR Pfam; PF01510; Amidase_2; 1. DR SMART; SM00644; Ami_2; 1. DR SMART; SM00701; PGRP; 1. DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1. PE 3: Inferred from homology; KW Antimicrobial; Bacteriolytic enzyme; Cytolysis; Host cell lysis by virus; KW Host cytoplasm; Hydrolase; Late protein; Metal-binding; KW Viral release from host cell; Zinc. FT INIT_MET 1 FT /note="Removed; by host" FT /evidence="ECO:0000250" FT CHAIN 2..151 FT /note="Endolysin" FT /id="PRO_0000164409" FT DOMAIN 11..132 FT /note="N-acetylmuramoyl-L-alanine amidase" FT /evidence="ECO:0000255" FT BINDING 18 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04111" FT BINDING 123 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04111" FT BINDING 131 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04111" FT SITE 47 FT /note="Essential for amidase activity and zinc hydrate FT coordination" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04111" SQ SEQUENCE 151 AA; 16874 MW; 2C0880FFC920DE9E CRC64; MAKVQFKPRA TTEAIFVHCS ATKPSQNVGV REIRQWHKEQ GWLDVGYHFI IKRDGTVEAG RDELAVGSHA KGYNHNSIGV CLVGGIDDKG KFDANFTPAQ MQSLRSLLVT LLAKYEGSVL RAHHDVAPKA CPSFDLKRWW EKNELVTSDR G //